1rmh

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[[Image:1rmh.gif|left|200px]]
[[Image:1rmh.gif|left|200px]]
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{{Structure
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|PDB= 1rmh |SIZE=350|CAPTION= <scene name='initialview01'>1rmh</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1rmh", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1rmh| PDB=1rmh | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmh OCA], [http://www.ebi.ac.uk/pdbsum/1rmh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rmh RCSB]</span>
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'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''
'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''
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[[Category: Ke, H.]]
[[Category: Ke, H.]]
[[Category: Zhao, Y.]]
[[Category: Zhao, Y.]]
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[[Category: complex (isomerase/substrate)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:40:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:30:12 2008''
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Revision as of 04:40, 3 May 2008

Image:1rmh.gif

Template:STRUCTURE 1rmh

RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL


Overview

The crystal structure of human recombinant cyclophilin A complexed with a substrate of succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (AAPF) has been determined and refined to an R-factor of 0.189 at 2.4 A resolution. The structure revealed only the cis form of the substrate bound to cyclophilin A in a stoichiometry of 1:1. This binding ratio is different from the structure of cyclophilin A complexed with the tetrapeptide N-acetyl-Ala-Ala-Pro-Ala-amidomethylcourmarin. Model docking revealed that the trans form of AAPF does not fit into the active site. The observation that only the trans cis form of AAPF binds to cyclophilin A implies that cyclophilin A predominantly catalyzes the trans to cis isomerization of a peptidylprolyl amide bond. On the basis of the structure, it is proposed that Arg55 hydrogen-bonds to the nitrogen to deconjugate the resonance of the prolyl amide bond and thus facilitates the cis-trans rotation.

About this Structure

1RMH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7356-61. PMID:8652511 Page seeded by OCA on Sat May 3 07:40:20 2008

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